scholarly journals First record of genus Cryptonanus (Didelphimorphia) in the state of Rio de Janeiro, Brazil

Check List ◽  
2016 ◽  
Vol 12 (1) ◽  
pp. 1827 ◽  
Author(s):  
Ana Cláudia Delciellos ◽  
Maria Carolina Viana ◽  
Márcia Aguieiras ◽  
Fernando Chiaradia ◽  
Denise De Alemar Gaspar
Keyword(s):  
Von Willebrand Factor ◽  
Rio De Janeiro ◽  
First Record ◽  
Morphological Characters ◽  
Geographic Range ◽  
The State ◽  
Forest Fragment ◽  
Phylogenetic Reconstructions ◽  
Von Willebrand ◽  
Willebrand Factor

Here we report the first record of genus Cryptonanus in the state of Rio de Janeiro, Brazil. One specimen (MZUSP35409) was captured in an Atlantic Forest fragment and was identified by morphological characters and molecular analysis using cytochrome‑b (MT-CYB) and von Willebrand Factor (VWF). Phylogenetic reconstructions based on VWF sequences positioned our specimen into the genus Cryptonanus, and the shortest genetic distance of MT-CYB was estimated between our specimen and an undescribed specimen from Piauí. Our record increases the genus’ geographic range approximately 350 km from Cotia and Ibiúna municipalities, São Paulo. The genus Cryptonanus remains taxonomically poorly understood.

scholarly journals First record of the bat Mimon crenulatum (E. Geoffroy, 1801) (Mammalia: Chiroptera) in the state of Rio de Janeiro, Southeastern Brazil

2006 ◽  
Vol 66 (1b) ◽  
pp. 295-299 ◽  
Author(s):  
M. A. R. Mello ◽  
A. Pol
Keyword(s):  
Natural History ◽  
Atlantic Forest ◽  
Rio De Janeiro ◽  
First Record ◽  
Geographic Range ◽  
The State ◽  
Southeastern Brazil ◽  
Conservation Units

The present study reports an extension of the geographic range of the phyllostomid bat Mimon crenulatum. This is the first record of this species in the state of Rio de Janeiro, Southeastern Brazil. Bats were captured in two conservation units of the Atlantic Forest. Data on the ecology and morphometry of the individuals are presented and compared with data recorded for other localities. The occurrence of this bat species in the region, though new, is consistent with information on its natural history found in the literature.

Visualization of von Willebrand Factor Multimers by Enzyme-Conjugated Secondary Antibodies

1986 ◽  
Vol 55 (02) ◽  
pp. 276-278 ◽  
Author(s):  
F Brosstad ◽  
Inge Kjønniksen ◽  
B Rønning ◽  
H Stormorken
Keyword(s):  
Von Willebrand Factor ◽  
Chromogenic Substrate ◽  
Agarose Electrophoresis ◽  
Secondary Antibodies ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Beta Galactosidase

SummaryA method for visualization of the multimeric forms of von Willebrand Factor (vWF) in plasma and platelets is described. The method is based upon: 1) Separation of the vWF multimers by SDS-agarose electrophoresis, 2) Subsequent blotting of the vWF multimers onto nitrocellulose, 3) Immunolocalization and visualization of the vWF pattern by the sequential incubation of the blot with a) primary vWF antiserum, b) peroxidase- or beta-galactosidase-conjugated secondary antibodies and a relevant chromogenic substrate.

Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

1988 ◽  
Vol 60 (02) ◽  
pp. 182-187 ◽  
Author(s):  
Morio Aihara ◽  
Ken Tamura ◽  
Ryuko Kawarada ◽  
Keizou Okawa ◽  
Yutaka Yoshida
Keyword(s):  
Platelet Aggregation ◽  
Von Willebrand Factor ◽  
Ricinus Communis ◽  
Protein S ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Normal Plasma ◽  
Ricinus Communis Agglutinin ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryThe adhesion of human fixed washed platelets (FWP) to collagen was decreased after treatment with Serratia marcescens protease (SP), which removed 95% of the glycocalicin from platelet membrane glycoprotein (GP) lb. However, the diminished adhesion of SP treated FWP to collagen could still be increased in the presence of purified von Willebrand factor (vWF). This ability of vWF to increase FWP adhesion to collagen is defined as collagen cofactor (CCo). The adhesion of FWP to collagen was not affected by a monoclonal antibody (MAb) to GP Ilb/IIIa (10E5), that inhibits ADP and collagen induced platelet aggregation. On the other hand, it was decreased by 50% by a MAb to GP lb (6D1), that inhibits ristocetin induced platelet aggregation. Adhesion of FWP in buffer to collagen was completely inhibited by Ricinus communis agglutinin I or concanavalin A, while Lens culinalis agglutinin and wheat germ agglutinin showed 50% inhibition. The FWP adhesion to collagen in the presence of vWF (normal plasma) was unaffected by MAbs to GP Ilb/IIIa (10E5, P2, HPL1) but was decreased to 32-38% by MAbs to GP lb (6D1, AN51, HPL11). A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%. The MAb, CLB-RAg 201, that inhibits the binding of vWF to collagen, completely inhibited the CCo of normal plasma. In conclusion, our data suggest that (1) GP lb has a partial role in FWP adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo is partly mediated through GP lb; but (4) other platelet membrane protein(s) besides GP lb or GP Ilb/IIIa must also be involved in FWP-vWF-collagen interactions.

Luminography – an Alternative Assay for Detection of von Willebrand Factor Multimers

1988 ◽  
Vol 60 (02) ◽  
pp. 133-136 ◽  
Author(s):  
R Schneppenheim ◽  
H Plendl ◽  
U Budde
Keyword(s):  
Von Willebrand Factor ◽  
Gel Electrophoresis ◽  
Detection Methods ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Luminescence Assay ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryA luminescence assay was adapted for detection of von Willebrand factor multimers subsequent to SDS-agarose gel electrophoresis and electroblotting onto nitrocellulose. The method is as fast as chromogenic detection methods and appears to be as sensitive as autoradiography without the disadvantages of the latter.

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